Author(s): Holmgren A
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Abstract The recent high-resolution solution structures of human and Escherichia coli thioredoxin in their oxidized and reduced states support a catalytic model of protein disulfide reduction involving binding of a target protein and nucleophilic attack by the active-site Cys32 thiolate to form a transition state mixed disulfide.
This article was published in Structure
and referenced in Journal of Clinical & Experimental Pathology